Thermolysin



Thermolysin (TML) is a thermostable metalloproteinase enzyme from Bacillus thermoproteolyticus. It catalyzes the hydrolysis of peptide bonds containing hydrophobic residues. The images at the left and at the right correspond to one representative Thermolysin (3dnz). See Metalloproteases and Matrix metalloproteinase for discussion.

3D Structures of Thermolysin
Update June 2011

Thermolysin
2whz, 3fvp, 3dnz, 3do0, 3do1, 3do2, 2g4z, 2a7g, 1gxw, 1kei, 1l3f, 1tlx, 2tlx, 8tln, 3p7p, 3p7q, 3p7r, 3p7s, 3p7t, 3p7u, 3p7v, 3p7w – TML

3ls7 - TML residues 233-548

1trl - TML residues 255-316 – NMR

3fxs, 3fbo, 3eim, 1lna, 1lnb, 1lnc, 1lnd, 1lne, 1lnf - TML residues 233-548+metal ion replacing Ca

TML+transition state analog
1tlp, 1tmn, 2tmn, 4tmn, 5tmn – TML+transition state analog

TML+ amino acid
1kl6 – TML+ alanine

TML+ dipeptide
2wi0, 3tmn – TML+ dipeptide

3fgd - TML residues 233-548+dipeptide

TML+inhibitor
1fjo, 1fj3, 1fjq, 1fjt, 1fju, 1fjv, 1fjw, 4tli, 5tli, 6tli, 7tli, 8tli, 1tli, 2tli, 3tli – TML soaked in organic solvents

3fv4, 3fxp, 3flf, 3fb0, 3fcq, 3f28, 3f2p – TML residues 233-548+inhibitor

3fwd, 3for, 1y3g, 1zdp, 1z9g, 1pes, 1pe7, 1pe8, 1os0, 1kto, 1ks7, 1kro, 1kr6, 1kkk, 1kjo, 1kjp, 1qf0, 1qf1, 1qf2, 1hyt, 1thl, 6tmn, 7tln, 4tln, 5tln, 1pe5, 3ms3, 3msa, 3msf, 3msn, 3n21, 3nn7 – TML+inhibitor